2qfd

Crystal structure of the regulatory domain of human RIG-I with bound Hg

Method: X-RAY DIFFRACTION Dmax: 131.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Probable ATP-dependent RNA helicase DDX58

Homo sapiens

UniProt O95786

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
10 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain J; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276
9 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 802–925 Fragment:Regulatory domain HG MERCURY (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES pH 10.0, 18% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.70 Å R-free 0.276

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

43 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDX58_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–145; UniProt 802–925 Author chain B; PDBConstruct 22–145; UniProt 802–925 Author chain C; PDBConstruct 22–145; UniProt 802–925 Author chain D; PDBConstruct 22–145; UniProt 802–925 Author chain E; PDBConstruct 22–145; UniProt 802–925 Author chain F; PDBConstruct 22–145; UniProt 802–925 Author chain G; PDBConstruct 22–145; UniProt 802–925 Author chain H; PDBConstruct 22–145; UniProt 802–925 Author chain I; PDBConstruct 22–145; UniProt 802–925 Author chain J; PDBConstruct 22–145; UniProt 802–925

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2qfd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qfd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qfd
Deposition date deposition_date2007-06-27
Structure title titleCrystal structure of the regulatory domain of human RIG-I with bound Hg
Keywords keywords;Zinc Finger, Alternative splicing, Antiviral defense, ATP-binding, Helicase, Hydrolase, Immune response, Innate immunity, Interferon induction, Nucleotide-binding, Polymorphism, RNA-binding, Ubl conjugation ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier43.83
Radius of gyration Rg (electron density) rg_electron43.33
Forward intensity I(0) i0300963000.00
Molecular weight molecular_weight143820.0 kDa
Excluded volume excluded_volume180100 ų
Envelope volume envelope_volume279200 ų
Hydration-shell volume shell_volume54239 ų
Envelope diameter envelope_diameter138.6
Shell Rg shell_rg48.95
Envelope Rg envelope_rg41.09
Shape Rg shape_rg43.32
Total Rg total_rg43.67
Total atoms total_atoms9990
Residues n_residues1210
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax131.5
Rg (real space) rg_real43.67
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real3.0100e+08
I(0) uncertainty (real space) i0_real_error5.0270e+06
Rg (reciprocal space) rg_reciprocal43.82
I(0) (reciprocal space) i0_reciprocal301000000.0000
Solution quality estimate total_estimate0.8829
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.4
Skewness Skewness skewness0.054
Kurtosis Kurtosis kurtosis-0.724
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14580000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.989; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.507

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd2qfda_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfdb_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfdc_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfdd_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfde_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfdf_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfdg_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfdh_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfdi_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd2qfdj_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like

CATH v4.4 (10 domains)

Domain ID domain_id2qfdA00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdB00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdC00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdD00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdE00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdF00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdG00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdH00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdI00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id2qfdJ00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain

8. Citations (1)

9. Files and Curves (10)